Deciphering the Mechanistic Basis for Perfluoroalkyl-Protein Interactions.

ABSTRACT: Although rarely used in nature, fluorine has emerged as an important elemental ingredient in the design of proteins with altered folding, stability, oligomerization propensities, and bioactivity. Adding to the molecular modification toolbox, here we report the ability of privileged perfluorinated amphiphiles to noncovalently decorate proteins to alter their conformational plasticity and potentiate their dispersion into fluorous phases. Employing a complementary suite of biophysical, in-silico and in-vitro approaches, we establish structure-activity relationships defining these phenomena and investigate their impact on protein structural dynamics and intracellular trafficking. Notably, we show that the lead compound, perfluorononanoic acid, is 10⁶ times more potent in inducing no

SUBMITTER: Lawanprasert A 

PROVIDER: S-EPMC10364144 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature